30AY
Structure of the soluble domain of chimeric Adenylyl cyclase 95 in complex with stimulatory G protein, ATPalphaS, and forskolin
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Adenylate cyclase type 9 | polymer | 1353 | 150860.3 | 1 | UniProt (O60503) | Homo sapiens (human) | ATP pyrophosphate-lyase 9,Adenylate cyclase type IX,ACIX,Adenylyl cyclase 9,AC9 |
| 2 | B (B) | Guanine nucleotide-binding protein G(s) subunit alpha | polymer | 404 | 46988.8 | 1 | Trichoplusia ni | ||
| 3 | C (A) | FORSKOLIN | non-polymer | 410.5 | 1 | Chemie (FOK) PubChem (47936) | |||
| 4 | D (A) | ADENOSINE-5'-SP-ALPHA-THIO-TRIPHOSPHATE | non-polymer | 523.2 | 1 | Chemie (T99) | |||
| 5 | E (B) | 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE | non-polymer | 539.2 | 1 | Chemie (GSP) | |||
| 6 | F (B) | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) PubChem (888) |
Sequence modifications
A: 1 - 1353 (UniProt: O60503)
| PDB | External Database | Details |
|---|---|---|
| Glu 401 | Val 401 | engineered mutation |
| Ala 407 | Ser 407 | engineered mutation |
| Ile 440 | Thr 440 | engineered mutation |
| Thr 515 | Asn 515 | engineered mutation |
| His 519 | Leu 519 | engineered mutation |
| Ala 522 | Gln 522 | engineered mutation |
| Tyr 562 | Gln 562 | engineered mutation |
| Leu 1082 | Tyr 1082 | engineered mutation |
| Ser 1112 | Ala 1112 | engineered mutation |
| Val 1173 | Thr 1173 | engineered mutation |
| Asn 1189 | Asp 1189 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 197849.1 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 1497.3 | |
| All* | Total formula weight | 199346.4 |
